Tracer diffusion coefficients of oxyhemoglobin a and oxyhemoglobin s in blood cells as determined by pulsed field gradient NMR |
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Authors: | Cherie H. Everhart Don A. Gabriel Charles S. Johnson |
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Affiliation: | 1. Department of Chemistry, University of North Carolina, Chapel Hill, NC 27514, U.S.A.;2. Department of Medicine, University of North Carolina, Chapel Hill, NC 27514, U.S.A. |
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Abstract: | It is demonstrated that tracer diffusion coefficients can be determined for oxyhemoglobin A (HbA-O2) and oxyhemoglobin S (HbS-O2) in intact blood cells by means of pulsed field gradient NMR (PFG-NMR). This is possible because the method discriminates between both rapidly moving water molecules and molecules having small proton transverse relaxation times (T2). The results indicate that only hemoglobin molecules contribute to the echo signals when large field gradients are used. The dependence of the measured diffusion coefficients on osmolarity and pH are attributed to changes in hemoglobin concentration resulting from changes in cell volume. |
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Keywords: | NMR Diffusion Hemoglobin Hemoglobin S |
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